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Conserved domains on  [gi|1948811128|gb|QQD25248|]
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DUF3393 domain-containing protein [Venatoribacter cucullus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 202-362 1.27e-96

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


:

Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 284.45  E-value: 1.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 202 PIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEKLLTGAELFRPETNIELGCA 281
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 282 YLNILDTQYLAAVKDPQSRLYCVIAAYNTGAGNVARSFTGNtsVRDAAPRINALSPTQVYAHLRRRLPYEETRNYLEKVN 361
Cdd:cd16893    81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSD--RKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVL 158


                  .
gi 1948811128 362 K 362
Cdd:cd16893   159 K 159
Mltc_N super family cl13335
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 58-119 8.20e-04

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


The actual alignment was detected with superfamily member pfam11873:

Pssm-ID: 432150  Cd Length: 161  Bit Score: 39.54  E-value: 8.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948811128  58 YRDYRQQLEKVWSKPEL--SDKKVWVEYSDNLRTRRTVDFERNEVRLS--FTGEEAARLSDARIRA 119
Cdd:pfam11873  12 VGQFSGNIEKIWGKNEVlvASKKDYVKYTDNYKSRAHIDFDKGIITIEtlATKNPKAHLRNAIITT 77
 
Name Accession Description Interval E-value
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 202-362 1.27e-96

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 284.45  E-value: 1.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 202 PIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEKLLTGAELFRPETNIELGCA 281
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 282 YLNILDTQYLAAVKDPQSRLYCVIAAYNTGAGNVARSFTGNtsVRDAAPRINALSPTQVYAHLRRRLPYEETRNYLEKVN 361
Cdd:cd16893    81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSD--RKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVL 158


                  .
gi 1948811128 362 K 362
Cdd:cd16893   159 K 159
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
181-368 1.27e-57

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 191.42  E-value: 1.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 181 VVTITIPLNRDAVPQRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAwGK 260
Cdd:PRK11671  173 IYSVTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMK-GK 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 261 EKLLTGAELFRPETNIELGCAYLNILDTQYLAAVKDPQSRLYCVIAAYNTGAGNVARSFTGNTSvrDAAPRINALSPTQV 340
Cdd:PRK11671  252 SGQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKI--QAANIINTMSPGDV 329

                         170       180
                  ....*....|....*....|....*...
gi 1948811128 341 YAHLRRRLPYEETRNYLEKVNKSLTTYK 368
Cdd:PRK11671  330 YQTLTTRHPSAESRRYLYKVNTAQKSYR 357
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 109-369 2.24e-38

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 137.43  E-value: 2.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 109 AARLSDARIRAEFEKVINASLEQAYKADPVLARTGGAQPPASRQPVAGIKPEQITELLQQARQQQQRTGKGEVVTITIPL 188
Cdd:COG0741    12 ALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 189 NRDAVPQRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEKlltgAE 268
Cdd:COG0741    92 LAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLGPSP----DD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 269 LFRPETNIELGCAYLNILDTQYLAavkdpqsRLYCVIAAYNTGAGNVARSFTGNtsvRDAAPRInalsptqvyahlrrrL 348
Cdd:COG0741   168 LFDPETNIRAGAAYLRELLDRFDG-------DLVLALAAYNAGPGRVRRWLRRN---GDRDGEI---------------I 222

                         250       260
                  ....*....|....*....|.
gi 1948811128 349 PYEETRNYLEKVNKSLTTYKA 369
Cdd:COG0741   223 PYAETRNYVKKVLANYAIYRA 243
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 208-317 2.77e-26

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 101.23  E-value: 2.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 208 AQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEklltgaELFRPETNIELGCAYLNILD 287
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVD------DLFDPEKNIKAGTKYLKELY 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1948811128 288 TQYLAavkdpqsRLYCVIAAYNTGAGNVAR 317
Cdd:pfam01464  79 KQYGG-------DLWLALAAYNAGPGRVRK 101
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 58-119 8.20e-04

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 39.54  E-value: 8.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948811128  58 YRDYRQQLEKVWSKPEL--SDKKVWVEYSDNLRTRRTVDFERNEVRLS--FTGEEAARLSDARIRA 119
Cdd:pfam11873  12 VGQFSGNIEKIWGKNEVlvASKKDYVKYTDNYKSRAHIDFDKGIITIEtlATKNPKAHLRNAIITT 77
 
Name Accession Description Interval E-value
LT_MltC_MltE cd16893
membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and ...
 202-362 1.27e-96

membrane-bound lytic murein transglycosylases MltC and MltE, and similar proteins; MltC and MltE are periplasmic, outer membrane attached lytic transglycosylases (LTs), which cleave beta-1,4-glycosidic bonds joining N-acetylmuramic acid and N-acetylglucosamine in the cell wall peptidoglycan, yielding 1,6-anhydromuropeptides. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda


Pssm-ID: 381614 [Multi-domain]  Cd Length: 162  Bit Score: 284.45  E-value: 1.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 202 PIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEKLLTGAELFRPETNIELGCA 281
Cdd:cd16893     1 PIVEKYAKKYGVDPALILAIIETESSFNPYAVSHSPAYGLMQIVPSTAGRDVYRLLGGKGGLPSKSYLFDPENNIDIGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 282 YLNILDTQYLAAVKDPQSRLYCVIAAYNTGAGNVARSFTGNtsVRDAAPRINALSPTQVYAHLRRRLPYEETRNYLEKVN 361
Cdd:cd16893    81 YLHILQNRYLKGIKNPKSREYCAIAAYNGGAGNVLRTFSSD--RKKAISKINRLSPDEVYQHLTKKLPAAETRNYLKKVL 158


                  .
gi 1948811128 362 K 362
Cdd:cd16893   159 K 159
mltC PRK11671
membrane-bound lytic murein transglycosylase MltC;
181-368 1.27e-57

membrane-bound lytic murein transglycosylase MltC;


Pssm-ID: 183271 [Multi-domain]  Cd Length: 359  Bit Score: 191.42  E-value: 1.27e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 181 VVTITIPLNRDAVPQRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAwGK 260
Cdd:PRK11671  173 IYSVTINMVPNHLDKRAHKYLPMVRKASRKYGVDESLILAIMQTESSFNPYAVSRSDALGLMQVVQHTAGKDVFRMK-GK 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 261 EKLLTGAELFRPETNIELGCAYLNILDTQYLAAVKDPQSRLYCVIAAYNTGAGNVARSFTGNTSvrDAAPRINALSPTQV 340
Cdd:PRK11671  252 SGQPSRSYLFDPANNIDTGTAYLAILQNVYLGGITNPTSRRYAVITAYNGGAGSVLRVFSNDKI--QAANIINTMSPGDV 329

                         170       180
                  ....*....|....*....|....*...
gi 1948811128 341 YAHLRRRLPYEETRNYLEKVNKSLTTYK 368
Cdd:PRK11671  330 YQTLTTRHPSAESRRYLYKVNTAQKSYR 357
MltE COG0741
Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin ...
 109-369 2.24e-38

Soluble lytic murein transglycosylase or regulatory protein s ( may contain LysM/invasin domain) [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440504 [Multi-domain]  Cd Length: 244  Bit Score: 137.43  E-value: 2.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 109 AARLSDARIRAEFEKVINASLEQAYKADPVLARTGGAQPPASRQPVAGIKPEQITELLQQARQQQQRTGKGEVVTITIPL 188
Cdd:COG0741    12 ALAASAAAALALALLAAAAAAAALAAAAAALAAAAAAAAGAAAAAASAAAGGPALAAALAAADALAAFAAIAALAAELLA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 189 NRDAVPQRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEKlltgAE 268
Cdd:COG0741    92 LAALLLRRPLPYLPLIEEAAKKYGVDPALVLALIRQESAFNPNAVSPAGARGLMQLMPATARRLGLKLGLGPSP----DD 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 269 LFRPETNIELGCAYLNILDTQYLAavkdpqsRLYCVIAAYNTGAGNVARSFTGNtsvRDAAPRInalsptqvyahlrrrL 348
Cdd:COG0741   168 LFDPETNIRAGAAYLRELLDRFDG-------DLVLALAAYNAGPGRVRRWLRRN---GDRDGEI---------------I 222

                         250       260
                  ....*....|....*....|.
gi 1948811128 349 PYEETRNYLEKVNKSLTTYKA 369
Cdd:COG0741   223 PYAETRNYVKKVLANYAIYRA 243
emtA PRK15470
membrane-bound lytic murein transglycosylase EmtA;
187-364 2.55e-36

membrane-bound lytic murein transglycosylase EmtA;


Pssm-ID: 185367 [Multi-domain]  Cd Length: 203  Bit Score: 130.86  E-value: 2.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 187 PLNRDAVPQRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRK-AWGKEKllT 265
Cdd:PRK15470   26 PWNAKVPVQRAMQWMPISQKAGAAWGVDPQLITAIIAIESGGNPNAVSKSNAIGLMQLKASTSGRDVYRRmGWSGEP--T 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 266 GAELFRPETNIELGCAYLNILDTQYLAAVKDPQSRLYCVIAAYNTGAGNVARSFTGNTsvRDAAPRINALSPTQVYAHLR 345
Cdd:PRK15470  104 TSELKNPERNISMGAAYLNILETGPLAGIEDPKVLQYALVVSYANGAGALLRTFSSDR--KKAISKINDLDADEFLEHVA 181

                         170
                  ....*....|....*....
gi 1948811128 346 RRLPYEETRNYLEKVNKSL 364
Cdd:PRK15470  182 RNHPAPQAPRYIYKLEQAL 200
LT_Slt70-like cd16896
uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized ...
 203-362 6.41e-32

uncharacterized lytic transglycosylase subfamily with similarity to Slt70; Uncharacterized lytic transglycosylase (LT) with a conserved sequence pattern suggesting similarity to the Slt70, a 70kda soluble lytic transglycosylase which also has an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381617 [Multi-domain]  Cd Length: 146  Bit Score: 117.23  E-value: 6.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 203 IVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAgrdatrkAWGKEKL----LTGAELFRPETNIEL 278
Cdd:cd16896     7 YIEKYAKEYGVDPLLVAAVIKVESNFNPNAVSSKGAIGLMQIMPETA-------EWIAEKLgledFSEDDLYDPETNIRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 279 GCAYLNILDTQYlaavkdpQSRLYCVIAAYNTGAGNVAR--SFTGNTSVRDAAPRInalsptqvyahlrrrlPYEETRNY 356
Cdd:cd16896    80 GTWYLSYLLKEF-------DGNLVLALAAYNAGPGNVDKwlKDGGWSGDGKTLDQI----------------PFPETRHY 136


                  ....*.
gi 1948811128 357 LEKVNK 362
Cdd:cd16896   137 VKKVLK 142
Slt70-like cd13401
70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the ...
 200-369 4.37e-30

70kDa soluble lytic transglycosylase (Slt70) and similar proteins; Catalytic domain of the 70kda soluble lytic transglycosylase (LT)-like proteins, which also have an N-terminal U-shaped U-domain and a linker L-domain. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381604 [Multi-domain]  Cd Length: 152  Bit Score: 112.57  E-value: 4.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 200 FLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAgRDATRKAwgKEKLLTGAELFRPETNIELG 279
Cdd:cd13401     6 YRDLVERAAKKNGLDPALVYAIIRQESAFDPDAVSPAGALGLMQLMPATA-KDVAKKL--GLPYYSPRDLFDPEYNIRLG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 280 CAYLNILDTQYlaavkdPQSRLYcVIAAYNTGAGNVARsFTGNTSVRDAAPRInalsptqvyahlrRRLPYEETRNYLEK 359
Cdd:cd13401    83 SAYLAELLDRF------DGNPVL-ALAAYNAGPGRVRR-WLKRRGDLDPDLWI-------------ETIPFSETRNYVKR 141

                         170
                  ....*....|
gi 1948811128 360 VNKSLTTYKA 369
Cdd:cd13401   142 VLENYVVYRA 151
SLT pfam01464
Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found ...
 208-317 2.77e-26

Transglycosylase SLT domain; This family is distantly related to pfam00062. Members are found in phages, type II, type III and type IV secretion systems.


Pssm-ID: 396169 [Multi-domain]  Cd Length: 114  Bit Score: 101.23  E-value: 2.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 208 AQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRKAWGKEklltgaELFRPETNIELGCAYLNILD 287
Cdd:pfam01464   5 AQKYGVDPSLLLAIAQQESGFNPKAVSKSGAVGLMQIMPSTAKRLGLRVNPGVD------DLFDPEKNIKAGTKYLKELY 78

                          90       100       110
                  ....*....|....*....|....*....|
gi 1948811128 288 TQYLAavkdpqsRLYCVIAAYNTGAGNVAR 317
Cdd:pfam01464  79 KQYGG-------DLWLALAAYNAGPGRVRK 101
LT-like cd00254
lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble ...
 215-360 1.36e-24

lytic transglycosylase(LT)-like domain; Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381594 [Multi-domain]  Cd Length: 111  Bit Score: 96.51  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 215 PALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAGRDATRkawgkekllTGAELFRPETNIELGCAYLNILDTQYlaav 294
Cdd:cd00254     1 PALVLAVIRVESGFNPRAVSPAGARGLMQLMPGTARDLGRR---------GVDDLFDPEENIRAGARYLRELLDRF---- 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948811128 295 kdpQSRLYCVIAAYNTGAGNVARsftgntsvrdaaprinalsptqvyAHLRRRLPYEETRNYLEKV 360
Cdd:cd00254    68 ---GGDLELALAAYNAGPGAVDR------------------------WGGGEVPPYKETRNYVQRV 106
MLTF-like cd13403
membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily ...
 204-369 2.78e-18

membrane-bound lytic murein transglycosylase F (MLTF) and similar proteins; This subfamily includes membrane-bound lytic murein transglycosylase F (MltF, murein lyase F) that degrades murein glycan strands. It is responsible for catalyzing the release of 1,6-anhydromuropeptides from peptidoglycan. Lytic transglycosylase catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do goose-type lysozymes. However, in addition, it also makes a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.


Pssm-ID: 381606 [Multi-domain]  Cd Length: 161  Bit Score: 81.04  E-value: 2.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 204 VKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAgrdatrKAWGKEklltgaELFRPETNIELGCAYL 283
Cdd:cd13403     1 FKKYAEKYGFDWRLLAAQAYQESRFNPNARSPAGARGLMQLMPSTA------RELGVN------DRLDPEQNIHAGAKYL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 284 NILDTQYlAAVKDPQSRLYCVIAAYNTGAGNV------ARSFTGNTSV-RDAAPRINALSPTQVYAHLR-RRLPYEETRN 355
Cdd:cd13403    69 RYLRDRF-PPDIDEPDRLKFALAAYNAGPGHVrdarrlAKKYGLNPNVwFDNVEVLPLLKSPYYDPVVKyGYARGRETVN 147

                         170
                  ....*....|....
gi 1948811128 356 YLEKVNKSLTTYKA 369
Cdd:cd13403   148 YVRNIRKYYDAYKQ 161
MltF COG4623
Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, ...
 192-368 6.54e-18

Membrane-bound lytic murein transglycosylase MltF [Cell wall/membrane/envelope biogenesis, Signal transduction mechanisms];


Pssm-ID: 443662 [Multi-domain]  Cd Length: 421  Bit Score: 84.34  E-value: 6.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 192 AVPQRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAgrdatrKAWGKEklltgaELFR 271
Cdd:COG4623   256 RIEGRLPPYDPLFEKYAEEYGLDWRLLAALAYQESHWNPRARSPTGARGLMQLMPATA------KELGVD------DRLD 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 272 PETNIELGCAYLNILDTQYLAAVKDPQsRLYCVIAAYNTGAGNV------ARSFTGNTSVRDaaprINALSPTQVYAHLR 345
Cdd:COG4623   324 PEQSIRAGAKYLRWLYDRFPEAIDEPD-RWWFALAAYNAGPGHVqdarrlAKKQGLDPDRWF----DVEKSQPKYYDTGY 398

                         170       180
                  ....*....|....*....|...
gi 1948811128 346 RRlPYeETRNYLEKVNKSLTTYK 368
Cdd:COG4623   399 AR-GR-ETVNYVPNIRAYYDIYK 419
PRK11619 PRK11619
lytic murein transglycosylase; Provisional
 213-360 3.18e-15

lytic murein transglycosylase; Provisional


Pssm-ID: 183236 [Multi-domain]  Cd Length: 644  Bit Score: 77.02  E-value: 3.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 213 VDPALVMAIIQNESSFNPMARSHIPAFGLMQIVPASAgrDATRKAWGKEKLLTGAELFRPETNIELGCAYLNILDTQYla 292
Cdd:PRK11619  492 IPQSYAMAIARQESAWNPKARSPVGASGLMQIMPGTA--THTVKMFSIPGYSSSSQLLDPETNINIGTSYLEYVYQQF-- 567

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1948811128 293 avkdPQSRLYCViAAYNTGAGNVarsftgNTSVRDAAPRINALSPTQvyahlrrRLPYEETRNYLEKV 360
Cdd:PRK11619  568 ----GNNRILAS-AAYNAGPGRV------RTWLGNSAGRIDAVAFVE-------SIPFSETRGYVKNV 617
LT_VirB1-like cd16892
VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up ...
 213-311 1.17e-06

VirB1-like subfamily; This subfamily includes VirB1 protein, one of twelve proteins making up type IV secretion systems (T4SS). T4SS are macromolecular assemblies generally composed of VirB1-11 and VirD4 proteins, and are used by bacteria to transport material across their membranes. VirB1 acts as a lytic transglycosylase (LT), and is important with respect to piercing the peptidoglycan layer in the periplasm. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381613 [Multi-domain]  Cd Length: 143  Bit Score: 47.54  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 213 VDPALVMAIIQNESSFNPMA-------RSHIPA--------------------FGLMQIvpasagrdatrkawGKEKL-- 263
Cdd:cd16892     9 VHPETLAAIVQVESGGNPYAigvnggkLSRQPKtkaeaiatarqliaaghnfdVGLGQI--------------NSRNLar 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1948811128 264 --LTGAELFRPETNIELGCAylnILDTQYLAAVK---DPQSRLYCVIAAYNTG 311
Cdd:cd16892    75 lgLTVEDVFDPCTNLKAGAT---ILTECYARAKKtggDGQAALRAALSCYNTG 124
MltD-like cd16894
Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases ...
 219-359 1.71e-06

Membrane-bound lytic murein transglycosylase D and similar proteins; Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381615 [Multi-domain]  Cd Length: 129  Bit Score: 46.74  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 219 MAIIqnESSFNPMARSHIPAFGLMQIVPASAgrdatrKAWGkekLLTGAEL---FRPETNIELGCAYLNILDTQYlaavK 295
Cdd:cd16894    13 LALV--ESGFNPDAVSSAGAAGLWQFMPATA------REYG---LRVDSWVderRDPEKSTRAAARYLKDLYKRF----G 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1948811128 296 DPqsrlYCVIAAYNTGAGNVARSftgntsvrdaaprINALSPTQVYAHLRRRLPyEETRNYLEK 359
Cdd:cd16894    78 DW----LLALAAYNAGEGRVRRA-------------IKRAGTDKWEDYYRLYLP-AETRRYVPK 123
GEWL cd01021
Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; ...
 195-315 4.28e-05

Goose egg-white lysozyme; Eukaryotic goose-type or G-type lysozyme (goose egg-white lysozyme; GEWL) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc). Mammals have two lysozymes. This family corresponds to human and mouse lysozyme G-like protein 2.


Pssm-ID: 381601 [Multi-domain]  Cd Length: 174  Bit Score: 43.74  E-value: 4.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 195 QRAQNFLPIVKQQAQKWRVDPALVMAIIQNESSF-NPMAR----SHIPAFGLMQIvpasagrD----ATRKAWGKekllt 265
Cdd:cd01021    32 NRLNKYKDCIKQVGKKLCIDPALIAAIISRESRAgAALDKngwgDHGNGFGLMQV-------DkryhPPKGAWDS----- 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1948811128 266 gaelfrpETNIELGCAYLnildTQYLAAVKD------PQSRLYCVIAAYNTGAGNV 315
Cdd:cd01021   100 -------EEHIEQATGIL----IDFIKTVQRkhpswsPEQQLKGGIAAYNAGVGNV 144
Slt35-like cd13399
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ...
 213-329 6.28e-05

Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).


Pssm-ID: 381602 [Multi-domain]  Cd Length: 108  Bit Score: 41.91  E-value: 6.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1948811128 213 VDPALVMAIIQNESSFNPMA-RSHIPAFGLMQIVPASA---GRDAtrKAWGKEKLLTGAELFRPETNielgcaYLNILDT 288
Cdd:cd13399     3 VPPGILAAILGVESGFGPNAgGSPAGAQGIAQFMPSTWkayGVDG--NGDGKADPFNPEDAIASAAN------YLCRHGW 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1948811128 289 QYLAAVKDPQSRlycVIAAYNTGAGNVARsftgntSVRDAA 329
Cdd:cd13399    75 DLNAFLGEDNFL---ALAAYNAGPGAYAN------AVLELA 106
LT_IagB-like cd13400
Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like ...
 211-244 9.90e-05

Escherichia coli invasion protein IagB and similar proteins; Lytic transglycosylase-like protein, similar to Escherichia coli invasion protein IagB. IagB is encoded within a pathogenicity island in Salmonella enterica and has been shown to degrade polymeric peptidoglycan. IagB-like invasion proteins are implicated in the invasion of eukaryotic host cells by bacteria. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Members of this family resemble the soluble and insoluble membrane-bound LTs in bacteria and the LTs in bacteriophage lambda.


Pssm-ID: 381603 [Multi-domain]  Cd Length: 109  Bit Score: 41.36  E-value: 9.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1948811128 211 WRVDPALVMAIIQNESSFNPMARSHIP----AFGLMQI 244
Cdd:cd13400     1 YGVPPRLLRAIAKVESGFNPNAINRNKngsyDIGLMQI 38
SLT_4 pfam19489
Transglycosylase SLT domain; This entry represents a set of SLT like domains found in ...
 204-234 3.03e-04

Transglycosylase SLT domain; This entry represents a set of SLT like domains found in proteobacteria. SLT domains are enzymes that degrade murein.


Pssm-ID: 466107  Cd Length: 184  Bit Score: 41.06  E-value: 3.03e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1948811128 204 VKQQAQKWRVDPALVMAIIQNESSFNPMARS 234
Cdd:pfam19489  38 AKDSERKWGVPVAVQMAIIYQESSFRHNARP 68
Mltc_N pfam11873
Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found ...
 58-119 8.20e-04

Membrane-bound lytic murein transglycosylase C, N-terminal domain; This domain is found associated with pfam01464. It is the N-terminal structural domain of MltC (Membrane-bound lytic murein transglycosylase C), one of the seven lytic transglycosylases found in the genome of the Gram-negative bacterium Escherichia coli. The role of the N-terminal domain is suggested to be important not as a mere structural extension of the active site beyond what is seen in other lytic transglycosylases but one that creates a peptide-binding site at position +2.


Pssm-ID: 432150  Cd Length: 161  Bit Score: 39.54  E-value: 8.20e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1948811128  58 YRDYRQQLEKVWSKPEL--SDKKVWVEYSDNLRTRRTVDFERNEVRLS--FTGEEAARLSDARIRA 119
Cdd:pfam11873  12 VGQFSGNIEKIWGKNEVlvASKKDYVKYTDNYKSRAHIDFDKGIITIEtlATKNPKAHLRNAIITT 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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